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Originally published In Press as doi:10.1074/jbc.M011282200 on January 19, 2001

J. Biol. Chem., Vol. 276, Issue 16, 13025-13033, April 20, 2001
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Exchangeability of N Termini in the Ligand-gated Porins of Escherichia coli*

Daniel C. Scott, Zhenghua Cao, Zengbiao Qi, Matthew Bauler, John D. Igo, Salete M. C. Newton, and Phillip E. KlebbaDagger

From the Department of Chemistry & Biochemistry, University of Oklahoma, Norman, Oklahoma 73019

The ferric siderophore transporters of the Gram-negative bacterial outer membrane manifest a unique architecture: Their N termini fold into a globular domain that lodges within, and physically obstructs, a transmembrane porin beta -barrel formed by their C termini. We exchanged and deleted the N termini of two such siderophore receptors, FepA and FhuA, which recognize and transport ferric enterobactin and ferrichrome, respectively. The resultant chimeric proteins and empty beta -barrels avidly bound appropriate ligands, including iron complexes, protein toxins, and viruses. Thus, the ability to recognize and discriminate these molecules fully originates in the transmembrane beta -barrel domain. Both the hybrid and the deletion proteins also transported the ferric siderophore that they bound. The FepA constructs showed less transport activity than wild type receptor protein, but the FhuA constructs functioned with turnover numbers that were equivalent to wild type. The mutant proteins displayed the full range of transport functionalities, despite their aberrant or missing N termini, confirming (Braun, M., Killmann, H., and Braun, V. (1999) Mol. Microbiol. 33, 1037-1049) that the globular domain within the pore is dispensable to the siderophore internalization reaction, and when present, acts without specificity during solute uptake. These and other data suggest a transport process in which siderophore receptors undergo multiple conformational states that ultimately expel the N terminus from the channel concomitant with solute internalization.

* This work was supported by National Science Foundation Grant MCB9709418 and National Institutes of Health Grant GM53836.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Tel.: 405-325-4969; Fax: 405-325-6111; E-mail: peklebba@ou.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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